Notice of Pre-AIA or AIA Status
The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
REQUIREMENT FOR UNITY OF INVENTION
2. As provided in 37 CFR 1.475(a), a national stage application shall relate to one invention only or to a group of inventions so linked as to form a single general inventive concept (“requirement of unity of invention”). Where a group of inventions is claimed in a national stage application, the requirement of unity of invention shall be fulfilled only when there is a technical relationship among those inventions involving one or more of the same or corresponding special technical features. The expression “special technical features” shall mean those technical features that define a contribution which each of the claimed inventions, considered as a whole, makes over the prior art.
The determination whether a group of inventions is so linked as to form a single general inventive concept shall be made without regard to whether the inventions are claimed in separate claims or as alternatives within a single claim. See 37 CFR 1.475(e).
When Claims Are Directed to Multiple Categories of Inventions:
As provided in 37 CFR 1.475 (b), a national stage application containing claims to different categories of invention will be considered to have unity of invention if the claims are drawn only to one of the following combinations of categories:
(1) A product and a process specially adapted for the manufacture of said product; or
(2) A product and a process of use of said product; or
(3) A product, a process specially adapted for the manufacture of the said product, and a use of the said product; or
(4) A process and an apparatus or means specifically designed for carrying out the said process; or
(5) A product, a process specially adapted for the manufacture of the said product, and an apparatus or means specifically designed for carrying out the said process.
Otherwise, unity of invention might not be present. See 37 CFR 1.475 (c).
Election/Restrictions
3. Restriction is required under 35 U.S.C. 121 and 372.
This application contains the following inventions or groups of inventions which are not so linked as to form a single general inventive concept under PCT Rule 13.1.
In accordance with 37 CFR 1.499, applicant is required, in reply to this action, to elect a single invention to which the claims must be restricted.
Group I, claim(s) 1-7, 13-14 and 18, drawn to a protein of a scFv type, comprising a first polypeptide chain and a second polypeptide chain joined by a ligand and having the formula of VH domain-peptide ligand-VL domain, wherein the VH comprises at least amino acids N173, Y176, K181, Y217, Y222 from SEQ ID NO:3 and the VL comprises at least amino acids K31, Y33, N35 from SEQ ID NO:3 and a composition comprising the claimed protein.
Group II, claim(s) 8-12, drawn to a polynucleotide comprising the nucleic acid sequence of SEQ ID NO:1, a vector comprising the claimed polynucleotide, a host cell comprising the claimed vector.
Group III, claim(s) 15-16, drawn to a method for treating a disease or condition that results directly or indirectly from a4b1 integrin activity comprising administering to a human the claimed protein or composition.
Group IV, claim(s) 17, drawn to an in vitro method to prognosticate a chronic inflammatory disease by detecting binding of the claimed protein to the cell, tissue or sample and quantifying expression of VLA-4.
4. The groups of inventions listed above do not relate to a single general inventive concept under PCT Rule 13.1 because, under PCT Rule 13.2, they lack the same or corresponding special technical features for the following reasons: Groups I-IV lack unity of invention because even though the inventions of these groups require the technical feature of a protein of a scFv type, comprising a first polypeptide chain and a second polypeptide chain joined by a ligand and having the formula of VH domain-peptide ligand-VL domain, wherein the VH comprises at least amino acids N173, Y176, K181, Y217, Y222 from SEQ ID NO:3 and the VL comprises at least amino acids K31, Y33, N35 from SEQ ID NO:3, this technical feature is not a special technical feature as it does not make a contribution over the prior art of WO2018017863 (as in IDS). As found in the International Search Report, the Invention of the Group I was found to have no special technical feature that defined the contribution over the prior art of WO2018017863. Therefore, claim 1 is anticipated by WO2018017863. Since the 1st claimed invention has no special technical feature, it cannot share a special technical feature with the other claimed inventions. Thus, Applicant’s inventions do not contribute a special technical feature when view over the prior art, they do not have a single inventive concept and so lack unity of invention.
Groups I-IV lack unity of invention because the groups do not share the same or corresponding technical feature. Group I is directed to a technical feature of a protein of a scFv type, comprising a first polypeptide chain and a second polypeptide chain joined by a ligand and having the formula of VH domain-peptide ligand-VL domain wherein the VH has the recited features, and a composition comprising the claimed protein. Group II is directed to a polynucleotide, a vector and a host cell comprising the claimed polynucleotide. Group III is directed to a technical feature of a method of treatment. Group IV is directed to a technical feature of a method of prognosis a chronic inflammatory disease. Therefore, the above Inventions do not share a common special technical feature as they comprise different steps and utilize different products, which demonstrates that each method has a different mode of operation and use of structurally and functionally divergent materials. For example, a method for treating patients does not have a same corresponding technical feature as that in a method of prognosis/diagnosis because the patients in the method of diagnosis/prognosis are not required in the method of treatment. Accordingly, Groups I-IV are not so linked by the same or a corresponding special technical feature within meaning of PCT Rule 13.1 so as to form a single general inventive concept.
5. Applicant is reminded that upon the cancellation of claims to a non-elected invention, the inventorship must be corrected in compliance with 37 CFR 1.48(a) if one or more of the currently named inventors is no longer an inventor of at least one claim remaining in the application. A request to correct inventorship under 37 CFR 1.48(a) must be accompanied by an application data sheet in accordance with 37 CFR 1.76 that identifies each inventor by his or her legal name and by the processing fee required under 37 CFR 1.17(i).
6. The examiner has required restriction between product or apparatus claims and process claims. Where applicant elects claims directed to the product/apparatus, and all product/apparatus claims are subsequently found allowable, withdrawn process claims that include all the limitations of the allowable product/apparatus claims should be considered for rejoinder. All claims directed to a nonelected process invention must include all the limitations of an allowable product/apparatus claim for that process invention to be rejoined.
In the event of rejoinder, the requirement for restriction between the product/apparatus claims and the rejoined process claims will be withdrawn, and the rejoined process claims will be fully examined for patentability in accordance with 37 CFR 1.104. Thus, to be allowable, the rejoined claims must meet all criteria for patentability including the requirements of 35 U.S.C. 101, 102, 103 and 112. Until all claims to the elected product/apparatus are found allowable, an otherwise proper restriction requirement between product/apparatus claims and process claims may be maintained. Withdrawn process claims that are not commensurate in scope with an allowable product/apparatus claim will not be rejoined. See MPEP § 821.04. Additionally, in order for rejoinder to occur, applicant is advised that the process claims should be amended during prosecution to require the limitations of the product/apparatus claims. Failure to do so may result in no rejoinder. Further, note that the prohibition against double patenting rejections of 35 U.S.C. 121 does not apply where the restriction requirement is withdrawn by the examiner before the patent issues. See MPEP § 804.01.
7. Any inquiry concerning this communication or earlier communications from the examiner should be directed to CHANG-YU WANG whose telephone number is (571)272-4521. The examiner can normally be reached on Monday-Thursday, 7:00am-5:30pm EST.
Examiner interviews are available via telephone, in-person, and video conferencing using a USPTO supplied web-based collaboration tool. To schedule an interview, applicant is encouraged to use the USPTO Automated Interview Request (AIR) at http://www.uspto.gov/interviewpractice.
If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Jeffrey Stucker can be reached on 571-272-0911. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
Information regarding the status of an application may be obtained from the Patent Application Information Retrieval (PAIR) system. Status information for published applications may be obtained from either Private PAIR or Public PAIR. Status information for unpublished applications is available through Private PAIR only. For more information about the PAIR system, see http://pair-direct.uspto.gov. Should you have questions on access to the Private PAIR system, contact the Electronic Business Center (EBC) at 866-217-9197 (toll-free). If you would like assistance from a USPTO Customer Service Representative or access to the automated information system, call 800-786-9199 (IN USA OR CANADA) or 571-272-1000.
Chang-Yu Wang
February 20, 2026
/CHANG-YU WANG/Primary Examiner, Art Unit 1675
DETAILED ACTION
Status of Application/Election/Restrictions
8. Applicant’s election without traverse of Group I (claims 1-7,13-14 and 18) directed to protein of scFv in the reply filed on January 29, 2026 is acknowledged.
The typographic error of claims 8-9 in the prior office action of restriction requirement is corrected. Claims 8-9 are directed to polynucleotides and vectors which are grouped in Group II. The corrected office action of restriction requirement is included and attached herein.
Claims 3-7, 13, 15, 17 and 18 are amended. Claims 1-18 are pending in this Application. Claims 8-12 and 15-17 are withdrawn without traverse from further consideration pursuant to 37 CFR 1.142(b) as being drawn to nonelected inventions, there being no allowable generic or linking claim. Election was made without traverse in the reply filed on January 29, 2026.
9. Claims 1-7, 13-14 and 18 are under examination in this office action.
Information Disclosure Statement
9. The listing of references in the specification is not a proper information disclosure statement. 37 CFR 1.98(b) requires a list of all patents, publications, or other information submitted for consideration by the Office, and MPEP § 609.04(a) states, "the list may not be incorporated into the specification but must be submitted in a separate paper." Therefore, unless the references have been cited by the examiner on form PTO-892, they have not been considered.
Specification
10. The disclosure is objected to because of the following informalities: The use of the term “SHuffler®”, “Cell Lytic®” (p. 88; p. 89 of the amended specification filed 01/29/2026), which is a trade name or a mark used in commerce, has been noted in this application. The term should be accompanied by the generic terminology; furthermore the term should be capitalized wherever it appears or, where appropriate, include a proper symbol indicating use in commerce such as ™, SM , or ® following the term.
Although the use of trade names and marks used in commerce (i.e., trademarks, service marks, certification marks, and collective marks) are permissible in patent applications, the proprietary nature of the marks should be respected and every effort made to prevent their use in any manner which might adversely affect their validity as commercial marks.
11. The disclosure is objected to because it contains an embedded hyperlink and/or other form of browser-executable code (see p.114-128 of the amended specification filed on 01/29/2206). Applicant is required to delete the embedded hyperlink and/or other form of browser-executable code; references to websites should be limited to the top-level domain name without any prefix such as http:// or other browser-executable code. See MPEP § 608.01. Appropriate correction is required.
Claim Objections
12. Claims 1-7, 13-14 and 18 are objected to because of the following informalities: there is no article “A”, “An” or “The” recited in claims 1-7, 13-14 and 18.
The recitation “the said protein” recited in claim 1 should be “the protein”. Appropriate correction is required.
Claim Rejections - 35 USC § 112
13. The following is a quotation of 35 U.S.C. 112(b):
(b) CONCLUSION.—The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the inventor or a joint inventor regards as the invention.
The following is a quotation of 35 U.S.C. 112 (pre-AIA ), second paragraph:
The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the applicant regards as his invention.
Claims 5, 7, 14 and 18 are rejected under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor, or for pre-AIA the applicant regards as the invention.
Claims 5, 7 and 18 are indefinite because:
i. Claim 5 recites the limitation "the binding peptide…" in line 2 of the claim. There is insufficient antecedent basis for this limitation in the claim.
ii. Regarding claims 7 and 18, the phrase "preferably " renders the claims indefinite because it is unclear whether the limitations following the phrase are part of the claimed invention. See MPEP § 2173.05(d).
iii. Claim 14 recites the limitation "the treatment or prognosis…" in lines 1-2 of the claim. There is insufficient antecedent basis for this limitation in the claim.
iv. Claim 18 is indefinite because the claim is a “use claim” and recites the limitation “Use of…for preparing a drug to treat or prognosticate chronic inflammation disease preferably multiple sclerosis”, which attempts to claim a process without setting forth any steps involved in the process because it merely recites a use without any active, positive steps delimiting how this use is actually practiced. Ex parte Erlich, 3 USPQ2d 1011 (Bd. Pat. App. & Inter. 1986).
Claim Rejections - 35 USC § 101
14. 35 U.S.C. 101 reads as follows:
Whoever invents or discovers any new and useful process, machine, manufacture, or composition of matter, or any new and useful improvement thereof, may obtain a patent therefor, subject to the conditions and requirements of this title.
Claim 18 is also rejected under 35 U.S.C. 101 because the disclosed invention is inoperative and therefore lacks utility. Claim 8 merely recites a use without any active, positive steps delimiting how this use is actually practiced.
Claim Rejections - 35 USC § 112
15. The following is a quotation of the first paragraph of 35 U.S.C. 112(a):
(a) IN GENERAL.—The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor or joint inventor of carrying out the invention.
The following is a quotation of the first paragraph of pre-AIA 35 U.S.C. 112:
The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor of carrying out his invention.
Claims 1-7, 13-14 and 18 are rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, as failing to comply with the written description requirement. The claim(s) contains subject matter which was not described in the specification in such a way as to reasonably convey to one skilled in the relevant art that the inventor or a joint inventor, or for pre-AIA the inventor(s), at the time the application was filed, had possession of the claimed invention.
To provide adequate written description and evidence of possession of a claimed genus, the specification must provide sufficient distinguishing identifying characteristics of the genus. The factors to be considered include disclosure of complete or partial structure, physical and/or chemical properties, functional characteristics, structure/function correlation, methods of making the claimed product, or any combination thereof.
Claims 1-7, 13-14 and 18 are drawn to a ScFv type protein comprising a structure of VH domain-peptide ligand-VL domain, wherein the VH comprises at least amino acids N173, Y176, K181, Y217, Y222 from SEQ ID NO:3 and the VL comprises at least amino acids K31, Y33, N35 from SEQ ID NO:3. Claims 2 and 3 encompass a genus of SCFv type protein comprising a structure of VH domain-peptide ligand-VL domain, wherein the VH comprises SEQ ID NOs:10-12 for HCDRs1-3 respectively and VL comprises SEQ ID NOs:7-9 for LCDRs1-3 or wherein the VH comprises aa Q117-S237 of SEQ ID NO:3 and the VL comprises aa D1-I111 of SEQ ID NO:3
The claims encompass a genus of structurally and functionally undefined ScFv type proteins comprising a genus of VH domain-a genus of peptide ligand-a genus of VL domain.
Applicant has not disclosed sufficient species for the broad genus of SCFv type protein comprising the claimed structure of VH domain-peptide ligand-VL domain and recited features.
The specification only describes an anti-VLA-4 scFv having a structure of a VH domain-peptide ligand-a VL domain, and comprising the amino acid sequence of instant SEQ ID NO:3 and binding to a4b1 integrin, and wherein the VH comprises SEQ ID NO: 5 (aa Q117-S237 of SEQ ID NO:3), the peptide ligand comprises SEQ ID NO:16 (-GGGGS-) and the VL comprises SEQ ID NO:6 (aa D1-I111 of SEQ ID NO:3).
However, the claims are not limited to the anti-VLA-4 scFv comprising SEQ ID NO:3 set forth above but also encompass structurally and functionally undefined ScFv type proteins comprising the structure of VH domain-peptide ligand-VL domain with no defined structural and functional sequences for the VH domain, peptide ligand and VL domain.
In making a determination of whether the application complies with the written description requirement of 35 U.S.C. 112, first paragraph, it is necessary to understand what Applicant is in possession of and what Applicant is claiming.
M.P.E.P. § 2163 instructs:
An invention described solely in terms of a method of making and/or its function may lack written descriptive support where there is no described or art-recognized correlation between the disclosed function and the structure(s) responsible for the function. . . .
An applicant may show possession of an invention by disclosure of drawings or structural chemical formulas that are sufficiently detailed to show that applicant was in possession of the claimed invention as a whole. . . .
An applicant may also show that an invention is complete by disclosure of sufficiently detailed, relevant identifying characteristics which provide evidence that applicant was in possession of the claimed invention, i.e., complete or partial structure, other physical and/or chemical properties, functional characteristics when coupled with a known or disclosed correlation between function and structure, or some combination of such characteristics.”
This standard has not been met in this case. From the specification, it is clear that Applicant is in possession of an anti-VLA-4 ScFv protein comprising the amino acid sequence SEQ ID NO:3 capable of binding to a4b1 integrin or VAL4. However, Applicant is not in possession of other structurally and functionally undefined ScFv type proteins comprising the structure of VH domain-peptide ligand-VL domain with no defined sequences for the VH domain, peptide ligand and VL domain. The specification provides no identification of any particular portion of the structure that must be conserved for the claimed genus of structurally and functionally undefined ScFv type protein comprising the structure of VH domain-peptide ligand-VL domain with no defined sequences for the VH domain, peptide ligand and VL domain.
In light of Amgen, Inc. v. Sanofi, 872 F.3d 1367 (Fed. Cir. 2017), describing a “fully characterized antigen” for an antibody is no longer adequate on its own to demonstrate possession of the antibody. Based on MPEP§2161.01 and 2163, the USPTO guidance regarding written description requirement of 35 U.S.C.§C112 (a), specifically concerning the written description requirement for claims drawn to antibodies and Federal Circuit decisions, when an antibody is claimed, 35USC112(a) requires adequate written description of the antibody itself. See Amgen 872 F.3d at 1378-79.
The court of the Federal Circuit also stressed that the “newly characterized antigen" test could not stand because it contradicted the quid pro quo of the patent system whereby one must describe an invention in order to obtain a patent. See Amgen, 872 F.3d at 1378-79, quoting Ariad Pharmaceuticals, Inc. v. Eli Lilly & Co., 598 F.3d 1336, 1345 (Fed. Cir.2010). In view of the Amgen decision, adequate written description of a newly characterized antigen alone should not be considered adequate written description of a claimed antibody to that newly characterized antigen, even when preparation of such an antibody is routine and conventional.
It is well established in the art that the formation of an intact antigen-binding site generally requires the association of the complete heavy and light chain variable regions of a given antibody, each of which consists of three CDRs which provide the majority of the contact residues for the binding of the antibody to its target epitope. The amino acid sequences and conformations of each of the heavy and light chain CDRs are critical in maintaining the antigen binding specificity and affinity which is characteristic of the parent immunoglobulin. It is expected that all of the heavy and light chain CDRs in their proper order and in the context of framework sequences which maintain their required conformation, are required in order to produce a protein having antigen-binding function and that proper association of heavy and light chain variable regions is required in order to form functional antigen binding sites. MacCallum et al. (J. Mol. Biol.,1996; 262: 732-745) teaches that although CDR3 of the heavy and light chain dominate, a number of residues outside the standard CDR definitions make antigen contacts (see p. 733, right col) and non-contacting residues within the CDRs coincide with residues as important in defining canonical backbone conformations (see page 735, left col.). Pascalis et al. (The Journal of Immunology, 2002; 169: 3076-3084) teaches that grafting of the CDRs into a human framework was performed by grafting CDR residues and maintaining framework residues that were deemed essential for preserving the structural integrity of the antigen binding site (see page 3079, right col.) and that although abbreviated CDR residues were used in the constructs, some residues in all 6 CDRs were used for the constructs (see page 3080, left col.). The fact that not just one CDR is essential for antigen binding or maintaining the conformation of the antigen binding site because although CDR H3 is at the center of most if not all antigen interactions, clearly other CDRs play an important role in the recognition process (page 199, left col.) and this is demonstrated in this work by using all CDRs except L2 and additionally using a framework residue located just before the H3 (see page 202, left col.; Casset et al., BBRC, 2003; 307: 198-205). Vajdos et al. (J. Mol. Biol. 2002; 320: 415-428) also teaches that antigen binding is primarily mediated by the CDRs more highly conserved framework segments which connect the CDRs are mainly involved in supporting the CDR loop conformations and in some cases framework residues also contact antigen (page 416, left col.). Holm et al. (Mol. Immunol., 2007; 44: 1075-1084) teaches that although residues in the CDR3 of the heavy chain were involved in antigen binding, unexpectedly a residue in CDR2 of the light chain was also involved (abstract). Chen et al. (J. Mol. Bio., 1999; 293: 865-881) teaches that the antigen binding site is almost entirely composed of residues from heavy chain CDRs, CDR-H1, H2, H3 (page 866). Wu et al. (J. Mol. Biol., 1999; 294:151-162) teaches that it is difficult to predict which framework residues serve a critical role in maintaining affinity and specificity due in part to the large conformational change in antibodies that accompany antigen binding (page 152 left col.) but certain residues have been identified as important for maintaining conformation. These references demonstrate that in order to generate an antibody or an ScFv with a specific binding activity or features, the antibody or ScFv must comprise all 6 CDRs with defined sequences or structures in order to maintain the antigen binding specificity and affinity.
However, The specification provides no structural and functional relationship between the claimed ScFv type protein and the binding specificity and affinity to a defined antigen except the anti-VLA-4 ScFv protein comprising the amino acid sequence SEQ ID NO:3 capable of binding to a4b1 integrin or VAL4 shown in Examples.
The instant specification fails to provide sufficient descriptive information, such as definitive structural or functional features of the claimed genus of ScFv type proteins comprising the structure of VH domain-peptide ligand-VL domain with no defined sequences for the VH domain, peptide ligand and VL domain. There is no description of the conserved regions which are critical to the function of the genus claimed. There is no description of the sites at which variability may be tolerated and there is no information regarding the relation of structure of other ScFv to the function of anti-VLA-4 ScFv protein comprising SEQ ID NO:3. Furthermore, the prior art does not provide compensatory structural or correlative teachings sufficient to enable one of skill to identify what other ScFv type proteins might be. Since the common characteristics/features of other ScFv type proteins are unknown, a skilled artisan cannot contemplate the functional correlations of the genus with the claimed invention. Accordingly, in the absence of sufficient recitation of distinguishing identifying characteristics, the specification does not provide adequate written description of the genus of ScFv type proteins.
Based on MPEP § 2161.01 and §2163, “to satisfy the written description requirement, a patent specification must describe the claimed invention in sufficient detail that one skilled in the art can reasonably conclude that the inventor had possession of the claimed invention. See, e.g., Moba, B.V. v. Diamond Automation, Inc., 325 F.3d 1306, 1319, 66 USPQ2d 1429, 1438 (Fed. Cir. 2003); Vas-Cath, Inc. v. Mahurkar, 935 F.2d at 1563, 19 USPQ2d at 1116”.
Vas-Cath Inc. v. Mahurkar, 19USPQ2d 1111, clearly states “applicant must convey with reasonable clarity to those skilled in the art that, as of the filing date sought, he or she was in possession of the invention. The invention is, for purposes of the ‘written description’ inquiry, whatever is now claimed.” (See page 1117.) The specification does not “clearly allow persons of ordinary skill in the art to recognize that [he or she] invented what is claimed.” (See Vas-Cath at page 1116).
As discussed above, the skilled artisan cannot envision the detailed chemical structure of the encompassed genus of ScFv type proteins comprising the structure of VH domain-peptide ligand-VL domain with no defined sequences for the VH domain, peptide ligand and VL domain, and therefore conception is not achieved until reduction to practice has occurred, regardless of the complexity or simplicity of the method of isolation. Adequate written description requires more than a mere statement that it is part of the invention and reference to a potential method of isolating it. The compound itself is required. See Fiers v. Revel, 25 USPQ2d 1601 at 1606 (CAFC 1993) and Amgen Inc. v. Chugai Pharmaceutical Co. Ltd., 18 USPQ2d 1016. One cannot describe what one has not conceived. See Fiddes v. Baird, 30 USPQ2d 1481 at 1483.
Therefore, the claimed ScFv type protein comprising the structure of VH domain-peptide ligand-VL domain with no defined sequences for the VH domain, peptide ligand and VL domain has not met the written description provision of 35 U.S.C. §112, first paragraph. Applicant is reminded that Vas-Cath makes clear that the written description provision of 35 U.S.C. §112 is severable from its enablement provision (see page 1115). Applicant is directed to the Guidelines for the Examination of Patent Applications Under the 35 U.S.C. 112, ¶ 1 "Written Description" Requirement. See MPEP § 2161.01 and 2163.
16. In the event the determination of the status of the application as subject to AIA 35 U.S.C. 102 and 103 (or as subject to pre-AIA 35 U.S.C. 102 and 103) is incorrect, any correction of the statutory basis for the rejection will not be considered a new ground of rejection if the prior art relied upon, and the rationale supporting the rejection, would be the same under either status.
Claim Rejections - 35 USC § 102
17. The following is a quotation of the appropriate paragraphs of 35 U.S.C. 102 that form the basis for the rejections under this section made in this Office action:
A person shall be entitled to a patent unless –
(a)(1) the claimed invention was patented, described in a printed publication, or in public use, on sale or otherwise available to the public before the effective filing date of the claimed invention.
(a)(2) the claimed invention was described in a patent issued under section 151, or in an application for patent published or deemed published under section 122(b), in which the patent or application, as the case may be, names another inventor and was effectively filed before the effective filing date of the claimed invention.
Claims 1, 4-7, 13-14 and 18 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Hu et al. (US20190309092, published Oct 10, 2019, priority Jul 21, 2016; also published as WO2018017863, as in IDS).
Claims 1, 4-7, 13-14 and 18 are drawn to a ScFv type protein comprising a structure of VH domain-peptide ligand-VL domain, wherein the VH domain comprises at least amino acids N173, Y176, K181, Y217 and Y222 from SEQ ID NO:3 and the VL domain comprises at least amino acids K31, Y33, N35 from SEQ ID NO:3. Dependent claims are directed to that the ligan is 5-15 amino acid in length including GGGGS (SEQ ID NO:16) (claims 4-5), bind to a4b1 integrin (claim 6), for use in treatment or prognosis of chronic inflammatory disease or multiple sclerosis (claims 7, 14 and 18), a composition comprising the claimed ScFv protein (claims 13-14).
Hu et al. (US20190309092) teaches a modified Fab single chain antibody protein comprising a structure of VL domain-linker (GGGGS)x-VH domain-CH1 and having the amino acid sequence of SEQ ID NO:12, wherein the VH comprises at least amino acids N173, Y176, K181, Y217 and Y222 from SEQ ID NO:3 and the VL domain comprises at least amino acids K31, Y33, N35 from SEQ ID NO:3 (see the sequence alignment below), and thus meets the limitations recited in instant claims 1, 4-7, 13-14 and 18 (see the sequence alignment below; paragraphs [0052]-[0054]; [0057], tables 1 and 9, claims 1-3, 9-14 and 49-54). The linker in the modified Fab single chain antibody disclosed by Hu contains –(GGGGS)x-(instant SEQ ID NO:16), which meets the limitations recited in claims 4-5 (see the sequence alignment below; paragraph [0057], table 1). Hu teaches a pharmaceutical composition comprising the modified Fab single chain antibody protein and a pharmaceutically acceptable excipient (see paragraph [0021]; [0042]-[0043], claims 49-54). The modified Fab single chain antibody protein disclosed by Hu can bind to a4b1 integrin recited in claim 6 and can be used for use in treatment or prognosis of chronic inflammatory disease or multiple sclerosis as in claims 7, 14 and 18 because the modified Fab single chain antibody protein disclosed by Hu meets the limitations recited in claims and has the same structure and comprise the same sequences as the instantly claimed scFv type protein. If the claimed scFv type protein can bind to a4b1 integrin and can be used for use in treatment or prognosis of chronic inflammatory disease or multiple sclerosis, the modified Fab single chain antibody protein disclosed by Hu having the same structure and sequences recited in instant claims can also bind to a4b1 integrin and can be used for use in treatment or prognosis of chronic inflammatory disease or multiple sclerosis. Thus, claims 1, 4-7, 13-14 and 18 are anticipated by Hu et al. (US20190309092).
The sequence search results disclose as follows:
SEQ ID NO:3
US-16-318-615-12
Sequence 12, US/16318615
Publication No. US20190309092A1
GENERAL INFORMATION
APPLICANT: Hu, Chih-Yung
APPLICANT: Huang, Chao-Yang
APPLICANT: Chen, Yu-Jung
APPLICANT: Wu, Chia-Cheng
APPLICANT: Kuan, Chien-Tsun
APPLICANT: Lo, Chia-Hsiang
APPLICANT: Tsai, Hsien-yu
TITLE OF INVENTION: MODIFIED ANTIGEN-BINDING FAB FRAGMENTS AND ANTIGEN-BINDING
TITLE OF INVENTION: MOLECULES COMPRISING THE SAME
FILE REFERENCE: D62975/PC0095
CURRENT APPLICATION NUMBER: US/16/318,615
CURRENT FILING DATE: 2019-01-17
PRIOR APPLICATION NUMBER: US 62/364,854
PRIOR FILING DATE: 2016-07-21
NUMBER OF SEQ ID NOS: 17
SEQ ID NO 12
LENGTH: 578
TYPE: PRT
ORGANISM: Artificial Sequence
FEATURE:
OTHER INFORMATION: VL1-Linker-VH1-CH1-CH2-CH3(Knob)
Query Match 94.6%; Score 1189; Length 578;
Best Local Similarity 92.0%;
Matches 229; Conservative 0; Mismatches 8; Indels 12; Gaps 1;
Qy 1 DVVMTQSPLSLPVTPGEPASISCRSSQSLAKSYSNTYLSWYLQKPGQSPQLLIYGIGNGG 60
||||||||||||||||||||||||||||||||| |||||||||||||||||||||| |
Db 1 DVVMTQSPLSLPVTPGEPASISCRSSQSLAKSYGNTYLSWYLQKPGQSPQLLIYGISNRF 60
Qy 61 SGVPARFSGSGSGTDFTLLISRVEAEDVGVYYCLQGTHQPYTFGQGTKVEI--------- 111
|||| ||||||||||||| ||||||||||||||||||||||||||||||||
Db 61 SGVPDRFSGSGSGTDFTLKISRVEAEDVGVYYCLQGTHQPYTFGQGTKVEIKRCGGGSGG 120
Qy 112 ---GGGGSQVQLVQSGAEVKKPGASVKVSCKGSGYTFTSYWMHWVRQAPGQRLEWIGEIG 168
||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 121 GGSGGGGSQVQLVQSGAEVKKPGASVKVSCKGSGYTFTSYWMHWVRQAPGQRLEWIGEID 180
Qy 169 PSESNTNYNQKFKGRVTLTVDISASTAYMELSSLRSEDTAVYYCARGGYAGWDYAIDYWG 228
||||||||||||||||||||||||||||||||||||||||||||||||| ||||||||||
Db 181 PSESNTNYNQKFKGRVTLTVDISASTAYMELSSLRSEDTAVYYCARGGYDGWDYAIDYWG 240
Qy 229 QGTLVTVSS 237
|||||||||
Db 241 QGTLVTVSS 249
SEQ ID NO:5-SEQ ID NO:6
US-16-318-615-12
Sequence 12, US/16318615
Publication No. US20190309092A1
GENERAL INFORMATION
APPLICANT: Hu, Chih-Yung
APPLICANT: Huang, Chao-Yang
APPLICANT: Chen, Yu-Jung
APPLICANT: Wu, Chia-Cheng
APPLICANT: Kuan, Chien-Tsun
APPLICANT: Lo, Chia-Hsiang
APPLICANT: Tsai, Hsien-yu
TITLE OF INVENTION: MODIFIED ANTIGEN-BINDING FAB FRAGMENTS AND ANTIGEN-BINDING
TITLE OF INVENTION: MOLECULES COMPRISING THE SAME
FILE REFERENCE: D62975/PC0095
CURRENT APPLICATION NUMBER: US/16/318,615
CURRENT FILING DATE: 2019-01-17
PRIOR APPLICATION NUMBER: US 62/364,854
PRIOR FILING DATE: 2016-07-21
NUMBER OF SEQ ID NOS: 17
SEQ ID NO 12
LENGTH: 578
TYPE: PRT
ORGANISM: Artificial Sequence
FEATURE:
OTHER INFORMATION: VL1-Linker-VH1-CH1-CH2-CH3(Knob)
Query Match 94.8%; Score 1165.3; Length 578;
Best Local Similarity 90.0%;
Matches 224; Conservative 0; Mismatches 8; Indels 17; Gaps 1;
Qy 1 DVVMTQSPLSLPVTPGEPASISCRSSQSLAKSYSNTYLSWYLQKPGQSPQLLIYGIGNGG 60
||||||||||||||||||||||||||||||||| |||||||||||||||||||||| |
Db 1 DVVMTQSPLSLPVTPGEPASISCRSSQSLAKSYGNTYLSWYLQKPGQSPQLLIYGISNRF 60
Qy 61 SGVPARFSGSGSGTDFTLLISRVEAEDVGVYYCLQGTHQPYTFGQGTKVEI--------- 111
|||| ||||||||||||| ||||||||||||||||||||||||||||||||
Db 61 SGVPDRFSGSGSGTDFTLKISRVEAEDVGVYYCLQGTHQPYTFGQGTKVEIKRCGGGSGG 120
Qy 112 --------QVQLVQSGAEVKKPGASVKVSCKGSGYTFTSYWMHWVRQAPGQRLEWIGEIG 163
|||||||||||||||||||||||||||||||||||||||||||||||||||
Db 121 GGSGGGGSQVQLVQSGAEVKKPGASVKVSCKGSGYTFTSYWMHWVRQAPGQRLEWIGEID 180
Qy 164 PSESNTNYNQKFKGRVTLTVDISASTAYMELSSLRSEDTAVYYCARGGYAGWDYAIDYWG 223
||||||||||||||||||||||||||||||||||||||||||||||||| ||||||||||
Db 181 PSESNTNYNQKFKGRVTLTVDISASTAYMELSSLRSEDTAVYYCARGGYDGWDYAIDYWG 240
Qy 224 QGTLVTVSS 232
|||||||||
Db 241 QGTLVTVSS 249
SEQ ID NO:7-SEQ ID NO:8-SEQ ID NO:9
US-16-318-615-12
Sequence 12, US/16318615
Publication No. US20190309092A1
GENERAL INFORMATION
APPLICANT: Hu, Chih-Yung
APPLICANT: Huang, Chao-Yang
APPLICANT: Chen, Yu-Jung
APPLICANT: Wu, Chia-Cheng
APPLICANT: Kuan, Chien-Tsun
APPLICANT: Lo, Chia-Hsiang
APPLICANT: Tsai, Hsien-yu
TITLE OF INVENTION: MODIFIED ANTIGEN-BINDING FAB FRAGMENTS AND ANTIGEN-BINDING
TITLE OF INVENTION: MOLECULES COMPRISING THE SAME
FILE REFERENCE: D62975/PC0095
CURRENT APPLICATION NUMBER: US/16/318,615
CURRENT FILING DATE: 2019-01-17
PRIOR APPLICATION NUMBER: US 62/364,854
PRIOR FILING DATE: 2016-07-21
NUMBER OF SEQ ID NOS: 17
SEQ ID NO 12
LENGTH: 578
TYPE: PRT
ORGANISM: Artificial Sequence
FEATURE:
OTHER INFORMATION: VL1-Linker-VH1-CH1-CH2-CH3(Knob)
Query Match 77.6%; Score 177; Length 578;
Best Local Similarity 46.3%;
Matches 38; Conservative 0; Mismatches 4; Indels 40; Gaps 2;
Qy 1 SCRSSQSLAKSYSNTYLSW-----------LIYGIGNGGSGVP----------------- 32
|||||||||||| |||||| ||||| | ||||
Db 22 SCRSSQSLAKSYGNTYLSWYLQKPGQSPQLLIYGISNRFSGVPDRFSGSGSGTDFTLKIS 81
Qy 33 ------------LQGTHQPYTF 42
||||||||||
Db 82 RVEAEDVGVYYCLQGTHQPYTF 103
SEQ ID NO:10-SEQ ID NO:11-SEQ ID NO:12
US-16-318-615-12
Sequence 12, US/16318615
Publication No. US20190309092A1
GENERAL INFORMATION
APPLICANT: Hu, Chih-Yung
APPLICANT: Huang, Chao-Yang
APPLICANT: Chen, Yu-Jung
APPLICANT: Wu, Chia-Cheng
APPLICANT: Kuan, Chien-Tsun
APPLICANT: Lo, Chia-Hsiang
APPLICANT: Tsai, Hsien-yu
TITLE OF INVENTION: MODIFIED ANTIGEN-BINDING FAB FRAGMENTS AND ANTIGEN-BINDING
TITLE OF INVENTION: MOLECULES COMPRISING THE SAME
FILE REFERENCE: D62975/PC0095
CURRENT APPLICATION NUMBER: US/16/318,615
CURRENT FILING DATE: 2019-01-17
PRIOR APPLICATION NUMBER: US 62/364,854
PRIOR FILING DATE: 2016-07-21
NUMBER OF SEQ ID NOS: 17
SEQ ID NO 12
LENGTH: 578
TYPE: PRT
ORGANISM: Artificial Sequence
FEATURE:
OTHER INFORMATION: VL1-Linker-VH1-CH1-CH2-CH3(Knob)
Query Match 85.6%; Score 222.6; Length 578;
Best Local Similarity 47.7%;
Matches 42; Conservative 0; Mismatches 2; Indels 44; Gaps 2;
Qy 1 SGYTFTSYWMH--------------EIGPSESNTNYNQKFKGRV---------------- 30
||||||||||| || ||||||||||||||||
Db 153 SGYTFTSYWMHWVRQAPGQRLEWIGEIDPSESNTNYNQKFKGRVTLTVDISASTAYMELS 212
Qy 31 --------------GGYAGWDYAIDYWG 44
||| ||||||||||
Db 213 SLRSEDTAVYYCARGGYDGWDYAIDYWG 240
Conclusion
18. NO CLAIM IS ALLOWED.
19. The prior art made of record and not relied upon is considered pertinent to applicant's disclosure.
Yuan et al. (Biochem J., 1996; 318:591-596, as in IDS) teach an anti-VLA-4 ScFv antibody sFv-195 comprising a structure of a VH-a linker (GGGGS)x-a VL-KDEL (see figure 1 below) and capable of binding , and wherein the VH and VL comprise the sequences of VH and VL from anti-a4 integrin antibody HP1/2 (see abstract; p.592, 1st col.), which comprises at least amino acids N173, Y176, K181, Y217 and Y222 from SEQ ID NO:3 and the VL domain comprises at least amino acids K31, Y33, N35 from SEQ ID NO:3 as evidenced by Hanf et al. (see p. 72, figure 1; Hanf et al., Methods, 2014; 65:68-76).
PNG
media_image1.png
246
752
media_image1.png
Greyscale
WO2018017863 (as in IDS) teaches a modified Fab single chain antibody protein comprising a structure of VL-linker-VH-CH1 and having the sequence of SEQ ID NO:12, which meets the limitations recited in claim 1 (see the sequence alignment below).
SEQ ID NO:3
BEY89577
ID BEY89577 standard; protein; 578 AA.
XX
AC BEY89577;
XX
DT 22-MAR-2018 (first entry)
XX
DE VL1-Linker-VH1-CH1-CH2-CH3(Knob) peptide construct, SEQ ID 12.
XX
KW antibody therapy; antimicrobial-gen.; cancer; cytostatic;
KW infectious disease; therapeutic.
XX
OS Synthetic.
OS Unidentified.
XX
CC PN WO2018017863-A1.
XX
CC PD 25-JAN-2018.
XX
CC PF 20-JUL-2017; 2017WO-US043126.
XX
PR 21-JUL-2016; 2016US-0364854P.
XX
CC PA (DCBU-) DCB-USA LLC.
CC PA (BIOT-) DEV CENT BIOTECHNOLOGY.
XX
CC PI Hu C, Huang C, Chen Y, Wu C, Kuan C, Lo C, Tsai H;
XX
DR WPI; 2018-07404W/11.
XX
CC PT New modified antigen-binding Fab fragment comprising light and heavy
CC PT chain variable domains and light and heavy chain constant domains, useful
CC PT for treating cancers and infectious diseases.
XX
CC PS Example 1; SEQ ID NO 12; 53pp; English.
XX
CC The present invention relates to a novel modified antigen-binding Fab
CC fragment, useful for treating cancers and infectious diseases. The
CC invention further relates to: (1) an antigen-binding molecule comprising
CC two or more of the antigen-binding Fab fragments defined above; (2) a
CC polynucleotide encoding the antigen-binding Fab fragment; (3) a vector
CC comprising polynucleotides encoding the antigen-binding Fab fragment; (4)
CC a host cell comprising the vector; and (5) a method for preparing the
CC antigen-binding molecule. The antigen-binding Fab fragment and the
CC antigen-binding molecule are useful for treating cancers, infectious
CC diseases, other diseases or disorders. The present sequence is a VL1-
CC Linker-VH1-CH1-CH2-CH3(Knob) peptide construct, useful for treating
CC diseases.
XX
SQ Sequence 578 AA;
Query Match 94.6%; Score 1189; Length 578;
Best Local Similarity 92.0%;
Matches 229; Conservative 0; Mismatches 8; Indels 12; Gaps 1;
Qy 1 DVVMTQSPLSLPVTPGEPASISCRSSQSLAKSYSNTYLSWYLQKPGQSPQLLIYGIGNGG 60
||||||||||||||||||||||||||||||||| |||||||||||||||||||||| |
Db 1 DVVMTQSPLSLPVTPGEPASISCRSSQSLAKSYGNTYLSWYLQKPGQSPQLLIYGISNRF 60
Qy 61 SGVPARFSGSGSGTDFTLLISRVEAEDVGVYYCLQGTHQPYTFGQGTKVEI--------- 111
|||| ||||||||||||| ||||||||||||||||||||||||||||||||
Db 61 SGVPDRFSGSGSGTDFTLKISRVEAEDVGVYYCLQGTHQPYTFGQGTKVEIKRCGGGSGG 120
Qy 112 ---GGGGSQVQLVQSGAEVKKPGASVKVSCKGSGYTFTSYWMHWVRQAPGQRLEWIGEIG 168
||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 121 GGSGGGGSQVQLVQSGAEVKKPGASVKVSCKGSGYTFTSYWMHWVRQAPGQRLEWIGEID 180
Qy 169 PSESNTNYNQKFKGRVTLTVDISASTAYMELSSLRSEDTAVYYCARGGYAGWDYAIDYWG 228
||||||||||||||||||||||||||||||||||||||||||||||||| ||||||||||
Db 181 PSESNTNYNQKFKGRVTLTVDISASTAYMELSSLRSEDTAVYYCARGGYDGWDYAIDYWG 240
Qy 229 QGTLVTVSS 237
|||||||||
Db 241 QGTLVTVSS 249
SEQ ID NO:7-SEQ ID NO:8-SEQ ID NO:9
BEY89577
ID BEY89577 standard; protein; 578 AA.
XX
AC BEY89577;
XX
DT 22-MAR-2018 (first entry)
XX
DE VL1-Linker-VH1-CH1-CH2-CH3(Knob) peptide construct, SEQ ID 12.
XX
KW antibody therapy; antimicrobial-gen.; cancer; cytostatic;
KW infectious disease; therapeutic.
XX
OS Synthetic.
OS Unidentified.
XX
CC PN WO2018017863-A1.
XX
CC PD 25-JAN-2018.
XX
CC PF 20-JUL-2017; 2017WO-US043126.
XX
PR 21-JUL-2016; 2016US-0364854P.
XX
CC PA (DCBU-) DCB-USA LLC.
CC PA (BIOT-) DEV CENT BIOTECHNOLOGY.
XX
CC PI Hu C, Huang C, Chen Y, Wu C, Kuan C, Lo C, Tsai H;
XX
DR WPI; 2018-07404W/11.
XX
CC PT New modified antigen-binding Fab fragment comprising light and heavy
CC PT chain variable domains and light and heavy chain constant domains, useful
CC PT for treating cancers and infectious diseases.
XX
CC PS Example 1; SEQ ID NO 12; 53pp; English.
XX
CC The present invention relates to a novel modified antigen-binding Fab
CC fragment, useful for treating cancers and infectious diseases. The
CC invention further relates to: (1) an antigen-binding molecule comprising
CC two or more of the antigen-binding Fab fragments defined above; (2) a
CC polynucleotide encoding the antigen-binding Fab fragment; (3) a vector
CC comprising polynucleotides encoding the antigen-binding Fab fragment; (4)
CC a host cell comprising the vector; and (5) a method for preparing the
CC antigen-binding molecule. The antigen-binding Fab fragment and the
CC antigen-binding molecule are useful for treating cancers, infectious
CC diseases, other diseases or disorders. The present sequence is a VL1-
CC Linker-VH1-CH1-CH2-CH3(Knob) peptide construct, useful for treating
CC diseases.
XX
SQ Sequence 578 AA;
Query Match 77.6%; Score 177; Length 578;
Best Local Similarity 46.3%;
Matches 38; Conservative 0; Mismatches 4; Indels 40; Gaps 2;
Qy 1 SCRSSQSLAKSYSNTYLSW-----------LIYGIGNGGSGVP----------------- 32
|||||||||||| |||||| ||||| | ||||
Db 22 SCRSSQSLAKSYGNTYLSWYLQKPGQSPQLLIYGISNRFSGVPDRFSGSGSGTDFTLKIS 81
Qy 33 ------------LQGTHQPYTF 42
||||||||||
Db 82 RVEAEDVGVYYCLQGTHQPYTF 103
SEQ ID NO:10-SEQ ID NO:11-SEQ ID NO:12
BEY89577
ID BEY89577 standard; protein; 578 AA.
XX
AC BEY89577;
XX
DT 22-MAR-2018 (first entry)
XX
DE VL1-Linker-VH1-CH1-CH2-CH3(Knob) peptide construct, SEQ ID 12.
XX
KW antibody therapy; antimicrobial-gen.; cancer; cytostatic;
KW infectious disease; therapeutic.
XX
OS Synthetic.
OS Unidentified.
XX
CC PN WO2018017863-A1.
XX
CC PD 25-JAN-2018.
XX
CC PF 20-JUL-2017; 2017WO-US043126.
XX
PR 21-JUL-2016; 2016US-0364854P.
XX
CC PA (DCBU-) DCB-USA LLC.
CC PA (BIOT-) DEV CENT BIOTECHNOLOGY.
XX
CC PI Hu C, Huang C, Chen Y, Wu C, Kuan C, Lo C, Tsai H;
XX
DR WPI; 2018-07404W/11.
XX
CC PT New modified antigen-binding Fab fragment comprising light and heavy
CC PT chain variable domains and light and heavy chain constant domains, useful
CC PT for treating cancers and infectious diseases.
XX
CC PS Example 1; SEQ ID NO 12; 53pp; English.
XX
CC The present invention relates to a novel modified antigen-binding Fab
CC fragment, useful for treating cancers and infectious diseases. The
CC invention further relates to: (1) an antigen-binding molecule comprising
CC two or more of the antigen-binding Fab fragments defined above; (2) a
CC polynucleotide encoding the antigen-binding Fab fragment; (3) a vector
CC comprising polynucleotides encoding the antigen-binding Fab fragment; (4)
CC a host cell comprising the vector; and (5) a method for preparing the
CC antigen-binding molecule. The antigen-binding Fab fragment and the
CC antigen-binding molecule are useful for treating cancers, infectious
CC diseases, other diseases or disorders. The present sequence is a VL1-
CC Linker-VH1-CH1-CH2-CH3(Knob) peptide construct, useful for treating
CC diseases.
XX
SQ Sequence 578 AA;
Query Match 85.6%; Score 222.6; Length 578;
Best Local Similarity 47.7%;
Matches 42; Conservative 0; Mismatches 2; Indels 44; Gaps 2;
Qy 1 SGYTFTSYWMH--------------EIGPSESNTNYNQKFKGRV---------------- 30
||||||||||| || ||||||||||||||||
Db 153 SGYTFTSYWMHWVRQAPGQRLEWIGEIDPSESNTNYNQKFKGRVTLTVDISASTAYMELS 212
Qy 31 --------------GGYAGWDYAIDYWG 44
||| ||||||||||
Db 213 SLRSEDTAVYYCARGGYDGWDYAIDYWG 240
SEQ ID NO:5-SEQ ID NO:6
BEY89577
ID BEY89577 standard; protein; 578 AA.
XX
AC BEY89577;
XX
DT 22-MAR-2018 (first entry)
XX
DE VL1-Linker-VH1-CH1-CH2-CH3(Knob) peptide construct, SEQ ID 12.
XX
KW antibody therapy; antimicrobial-gen.; cancer; cytostatic;
KW infectious disease; therapeutic.
XX
OS Synthetic.
OS Unidentified.
XX
CC PN WO2018017863-A1.
XX
CC PD 25-JAN-2018.
XX
CC PF 20-JUL-2017; 2017WO-US043126.
XX
PR 21-JUL-2016; 2016US-0364854P.
XX
CC PA (DCBU-) DCB-USA LLC.
CC PA (BIOT-) DEV CENT BIOTECHNOLOGY.
XX
CC PI Hu C, Huang C, Chen Y, Wu C, Kuan C, Lo C, Tsai H;
XX
DR WPI; 2018-07404W/11.
XX
CC PT New modified antigen-binding Fab fragment comprising light and heavy
CC PT chain variable domains and light and heavy chain constant domains, useful
CC PT for treating cancers and infectious diseases.
XX
CC PS Example 1; SEQ ID NO 12; 53pp; English.
XX
CC The present invention relates to a novel modified antigen-binding Fab
CC fragment, useful for treating cancers and infectious diseases. The
CC invention further relates to: (1) an antigen-binding molecule comprising
CC two or more of the antigen-binding Fab fragments defined above; (2) a
CC polynucleotide encoding the antigen-binding Fab fragment; (3) a vector
CC comprising polynucleotides encoding the antigen-binding Fab fragment; (4)
CC a host cell comprising the vector; and (5) a method for preparing the
CC antigen-binding molecule. The antigen-binding Fab fragment and the
CC antigen-binding molecule are useful for treating cancers, infectious
CC diseases, other diseases or disorders. The present sequence is a VL1-
CC Linker-VH1-CH1-CH2-CH3(Knob) peptide construct, useful for treating
CC diseases.
XX
SQ Sequence 578 AA;
Query Match 94.8%; Score 1165.3; Length 578;
Best Local Similarity 90.0%;
Matches 224; Conservative 0; Mismatches 8; Indels 17; Gaps 1;
Qy 1 DVVMTQSPLSLPVTPGEPASISCRSSQSLAKSYSNTYLSWYLQKPGQSPQLLIYGIGNGG 60
||||||||||||||||||||||||||||||||| |||||||||||||||||||||| |
Db 1 DVVMTQSPLSLPVTPGEPASISCRSSQSLAKSYGNTYLSWYLQKPGQSPQLLIYGISNRF 60
Qy 61 SGVPARFSGSGSGTDFTLLISRVEAEDVGVYYCLQGTHQPYTFGQGTKVEI--------- 111
|||| ||||||||||||| ||||||||||||||||||||||||||||||||
Db 61 SGVPDRFSGSGSGTDFTLKISRVEAEDVGVYYCLQGTHQPYTFGQGTKVEIKRCGGGSGG 120
Qy 112 --------QVQLVQSGAEVKKPGASVKVSCKGSGYTFTSYWMHWVRQAPGQRLEWIGEIG 163
|||||||||||||||||||||||||||||||||||||||||||||||||||
Db 121 GGSGGGGSQVQLVQSGAEVKKPGASVKVSCKGSGYTFTSYWMHWVRQAPGQRLEWIGEID 180
Qy 164 PSESNTNYNQKFKGRVTLTVDISASTAYMELSSLRSEDTAVYYCARGGYAGWDYAIDYWG 223
||||||||||||||||||||||||||||||||||||||||||||||||| ||||||||||
Db 181 PSESNTNYNQKFKGRVTLTVDISASTAYMELSSLRSEDTAVYYCARGGYDGWDYAIDYWG 240
Qy 224 QGTLVTVSS 232
|||||||||
Db 241 QGTLVTVSS 249
20. Any inquiry concerning this communication or earlier communications from the examiner should be directed to CHANG-YU WANG whose telephone number is (571)272-4521. The examiner can normally be reached on Monday-Thursday, 7:00am-5:00pm EST.
Examiner interviews are available via telephone, in-person, and video conferencing using a USPTO supplied web-based collaboration tool. To schedule an interview, applicant is encouraged to use the USPTO Automated Interview Request (AIR) at http://www.uspto.gov/interviewpractice.
If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Jeffrey Stucker can be reached on 571-272-0911. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
Information regarding the status of an application may be obtained from the Patent Application Information Retrieval (PAIR) system. Status information for published applications may be obtained from either Private PAIR or Public PAIR. Status information for unpublished applications is available through Private PAIR only. For more information about the PAIR system, see https://ppair-my.uspto.gov/pair/PrivatePair. Should you have questions on access to the Private PAIR system, contact the Electronic Business Center (EBC) at 866-217-9197 (toll-free). If you would like assistance from a USPTO Customer Service Representative or access to the automated information system, call 800-786-9199 (IN USA OR CANADA) or 571-272-1000.
Chang-Yu Wang
February 21, 2026
/CHANG-YU WANG/Primary Examiner, Art Unit 1675